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- W2160314300 abstract "Of the increasing number of sialidases found to be made by microorganisms, the trypanosome trans-sialidase is unique in its added ability to efficiently carry out a sialyltransferase reaction using preformed glycoconjugates. The enzyme is predicted to have a multidomain structure, with one domain containing sequence and expected structural features found in bacterial sialidases. The trans-sialidase is very similar in overall sequence to another trypanosome enzyme that has only sialidase activity. Hybrid expression constructs containing pieces of these trypanosome trans-sialidase and sialidase genes were used to determine which regions of trans-sialidase are required for sialyltransferase activity. Two domains were found to influence the enzymatic activity: the N-terminal catalytic domain, and a downstream domain that resembles an Fn3-like module." @default.
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- W2160314300 date "1997-01-01" @default.
- W2160314300 modified "2023-09-23" @default.
- W2160314300 title "Directed mutagenesis of the <i>Trypanosoma cruzi</i> trans-sialidase enzyme identifies two domains involved in its sialyltransferase activity" @default.
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- W2160314300 doi "https://doi.org/10.1093/glycob/7.3.445" @default.
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